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Biopolymers. 2017 Aug;107(8). doi: 10.1002/bip.23020.

Hydrophobic-hydrophilic forces in protein folding.

Author information

1
Laboratory of Cell Biology, National Cancer Institute; National Institutes of Health, Bethesda, Maryland, 20892.
2
Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem, 91904, Israel.

Abstract

The process of protein folding is obviously driven by forces exerted on the atoms of the amino-acid chain. These forces arise from interactions with other parts of the protein itself (direct forces), as well as from interactions with the solvent (solvent-induced forces). We present a statistical-mechanical formalism that describes both these direct and indirect, solvent-induced thermodynamic forces on groups of the protein. We focus on 2 kinds of protein groups, commonly referred to as hydrophobic and hydrophilic. Analysis of this result leads to the conclusion that the forces on hydrophilic groups are in general stronger than on hydrophobic groups. This is then tested and verified by a series of molecular dynamics simulations, examining both hydrophobic alkanes of different sizes and hydrophilic moieties represented by polar-neutral hydroxyl groups. The magnitude of the force on assemblies of hydrophilic groups is dependent on their relative orientation: with 2 to 4 times larger forces on groups that are able to form one or more direct hydrogen bonds.

KEYWORDS:

hydrophobic and hydrophilic forces and interactions; protein folding

PMID:
28387920
PMCID:
PMC5604469
DOI:
10.1002/bip.23020
[Indexed for MEDLINE]
Free PMC Article

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